Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q6YV23

Entry ID Method Resolution Chain Position Source
AF-Q6YV23-F1 Predicted AlphaFoldDB

No variants for Q6YV23

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6YV23

No associated diseases with Q6YV23

5 regional properties for Q6YV23

Type Name Position InterPro Accession
domain TolB, N-terminal 23 - 122 IPR007195
repeat WD40-like beta propeller 199 - 223 IPR011659-1
repeat WD40-like beta propeller 237 - 272 IPR011659-2
repeat WD40-like beta propeller 282 - 315 IPR011659-3
repeat WD40-like beta propeller 377 - 398 IPR011659-4

Functions

Description
EC Number 6.3.5.5 Carbon--nitrogen ligases with glutamine as amido-N-donor
Subcellular Localization
  • Plastid, chloroplast
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
carbamoyl-phosphate synthase complex A protein complex that catalyzes the formation of carbamoyl phosphate; comprises a small subunit that binds and cleaves glutamine, and a large subunit that accepts the ammonia group cleaved from glutamine, binds all of the remaining substrates and effectors, and carries out all of the other catalytic events.
chloroplast A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: 2 ATP + L-glutamine + CO2 + H2O = 2 ADP + phosphate + glutamate + carbamoyl phosphate.

5 GO annotations of biological process

Name Definition
'de novo' pyrimidine nucleobase biosynthetic process The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors.
'de novo' UMP biosynthetic process The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD(+) or oxygen.
arginine biosynthetic process The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
glutamine metabolic process The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.
nitrogen compound metabolic process The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
B9EXM2 CARB Carbamoyl-phosphate synthase large chain, chloroplastic Oryza sativa subsp japonica (Rice) PR
P49077 PYRB Aspartate carbamoyltransferase, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
Q9LVW7 CARA Carbamoyl-phosphate synthase small chain, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAAPPATASA PSLRPSAASP RAAAARSVAV PSGPRTVGPR RDGGRFLGVR AAKAVSGVQS
70 80 90 100 110 120
GTVVDDGVQR PWKLSDARLV LEDGSVWKAK SFGASGTQVG EVVFNTSLTG YQEILTDPSY
130 140 150 160 170 180
AGQFVLMTNP HIGNTGVNPD DEESNRCFLA GLIIRNLSIC TSNWRCTETL EEYLMKRNIM
190 200 210 220 230 240
GIYDVDTRAI TRRLREDGSL IGVLSTDQSR TDDELLEMAK NWKIVGVDLI SGVTCDAPYE
250 260 270 280 290 300
WSDKTDSEWE FKKGQSTESF HVVAYDFGIK HNILRRLTSY GCKITVVPAN WPASEVLNLK
310 320 330 340 350 360
PDGVFFSNGP GDPAAVPYAV KTVQEIIGKV PVFGICMGHQ LIGQALGGKT FKMKFGHHGG
370 380 390 400 410 420
NHPVCDLRSG RVDISAQNHN YAVDPESLPE GVKVTHINLN DNSCAGLQYP KMKLLSLQYH
430 440
PESSPGPHDS DLAFGEFIEM MKNNRL